Characterization of aminoacyl-tRNA synthetase stability and substrate interaction by differential scanning fluorimetry

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• 作者：Jamie A. Abbott^a ; ^{Jamie.Abbott@uvm.edu} ; Nathan M. Livingston^a ; Shawn B. Egri^a ; Ethan Guth^b ; Christopher S. Francklyn^a ; ^{Christopher.Francklyn@uvm.edu}
• 关键词：Differential scanning fluorimetry ; Aminoacyl-tRNA synthetase ; Histidyl-tRNA synthetase ; SYPRO Orange ; tRNA ; Amino acid
• 刊名：Methods
• 出版年：2017
• 出版时间：15 January 2017
• 年：2017
• 卷：113
• 期：Complete
• 页码：64-71
• 全文大小：987 K
• 卷排序：113

文摘

AARS protein stability can be evaluated by differential scanning fluorimetry (DSF). DSF can be used for determining the stability of AARS enzyme substitutions. AARS amino acid and inhibitor binding studies can be conducted with DSF. Thermal stability can change as a function of tRNA binding and be measured by DSF.